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sweet potato/tyrosine

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СтатииКлинични изследванияПатенти
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Phenolic constituents isolated from Fragaria ananassa Duch. inhibit antigen-stimulated degranulation through direct inhibition of spleen tyrosine kinase activation.

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We isolated eight phenolic constituents from Fragaria ananassa Duch. (strawberry) and determined their structures using 1D, 2D-NMR. Among the isolated compounds, linocinnamarin (LN), 1-O-trans-cinnamoyl-beta-d-glucopyranose (CG), and cinnamic acid (CA) exhibited antigen (Ag)-stimulated degranulation

Purification and characterization of p-coumaroyl-D-glucose hydroxylase of sweet potato (Ipomoea batatas) roots.

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p-Coumaroyl-D-glucose hydroxylase in sweet potato (Ipomoea batatas Lam.) has been purified to apparent electrophoretic homogeneity using a combination of anion-and cation-exchange, hydrophobic and gel filtration chromatography. The purified enzyme was a monomer with a molecular weight of 33,000 and

Purification and properties of phenylalanine ammonia-lyase in cut-injured sweet potato.

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L-Phenylalanine ammonia-lyase (PAL) activity was developed in response to cut injury in sweet potato root tissue. The enzyme was purified from tissue incubated for 1 day after slicing by ammonium sulfate fractionation, column chromatographies on L-phenylalanyl Sepharose 4B, phosphocellulose.

Inhibition of reactive nitrogen species in vitro and ex vivo by trypsin inhibitor from sweet potato 'Tainong 57' storage roots.

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Peroxynitrite (ONOO-), formed from a reaction of superoxide and nitric oxide, is one of the most potent cytotoxic species known to oxidize cellular constituents including essential proteins, lipids, and DNA. ONOO- induces cellular and tissue injury, resulting in several human diseases such as

Detection and Molecular Characterization of Boscalid-Resistant Botrytis cinerea Isolates from Strawberry.

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Botrytis cinerea isolates (n = 122) were collected from strawberry fields located in northern Greece during a 3-year period (2008-10) and tested for their sensitivity to the succinate dehydrogenase inhibitor boscalid. Sensitivity measurements showed three distinct phenotypes consisting of isolates

An arsenate reductase homologue possessing phosphatase activity from sweet potato (Ipomoea batatas [L.] Lam): kinetic studies and characterization.

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A cDNA encoding a putative arsenate reductase homologue (IbArsR) was cloned from sweet potato (Ib). The deduced protein showed a high level of sequence homology (16-66%) with ArsRs from other organisms. A 3-D homology structure was created based on AtArsR (PDB code 1T3K ) from Arabidopsis thaliana.

Effect of BTH on anthocyanin content and activities of related enzymes in Strawberry after harvest.

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The effect of benzo-thiadiazole-7-carbothioic acid S-methyl ester (BTH) at 0.2 g L(-1) on anthocyanin content and the enzymes involved in its metabolism such as glucose-6-phosphate dehydrogenase (G6PDH), shikimate dehydrogenase (SKDH), tyrosine ammonia lyase (TAL), phenylalanine ammonia lyase (PAL),

A novel serine protease from strawberry (Fragaria ananassa): Purification and biochemical characterization.

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In this study, a protease enzyme was purified from strawberry by using Sepharose-4B-l-tyrosine-p-amino benzoic acid affinity chromatography. The molecular weight of pure protease was determined 65.8 kDa by SDS-PAGE. The single band observed on the gel showed that the enzyme had a single polypeptide

Resistance to Pyraclostrobin and Boscalid in Botrytis cinerea Isolates from Strawberry Fields in the Carolinas.

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Botrytis cinerea, the causal agent of gray mold disease, is one of the most important plant-pathogenic fungi affecting strawberry. During the last decade, control of gray mold disease in the southeastern United States has largely been dependent on captan and the use of at-risk fungicides with

Blue light irradiation affects anthocyanin content and enzyme activities involved in postharvest strawberry fruit.

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Blue light irradiation was applied to postharvest strawberry fruit to explore its influence on anthocyanin content and anthocyanin biosynthetic enzyme activities. Strawberry fruit was irradiated with blue light at 40 μmol m(-2) s(-1) for 12 days at 5 °C. The results indicated that blue light

Delaying the biosynthesis of aromatic secondary metabolites in postharvest strawberry fruit exposed to elevated CO2 atmosphere.

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Aromatic secondary metabolites are closely related to quality attributes of postharvest fruit. In the present study, 20% CO2 was applied to strawberry fruit to investigate the regulation of elevated CO2 on aromatic secondary metabolites. The results showed that elevated

A tyrosinase with an abnormally high tyrosine hydroxylase/dopa oxidase ratio.

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The sequencing of the genome of Ralstonia solanacearum[Salanoubat M, Genin S, Artiguenave F, et al. (2002) Nature 415, 497-502] revealed several genes that putatively code for polyphenol oxidases (PPOs). This soil-borne pathogenic bacterium withers a wide range of plants. We detected the expression

Degradation of tyrosinase induced by phenylthiourea occurs following Golgi maturation.

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Tyrosinase, the rate-limiting enzyme of melanin synthesis, is a di-copper metalloprotein that catalyzes the conversion of L-tyrosine to L-DOPAquinone. Phenylthiourea (PTU) is a well-known inhibitor of tyrosinase and melanin synthesis and is known to interact with sweet potato catechol oxidase, an

Blood status and serum free amino acids in Papua New Guinea highlanders.

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Hematological values and serum amino-acid concentrations were measured in 17 healthy male adult Papua New Guinea highlanders who live on a sweet-potato staple diet. Hematological values were within the normal range, except for a low serum urea concentration. The concentrations of serum threonine,

Purification, enzymatic properties, and active site environment of a novel manganese(III)-containing acid phosphatase.

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A new manganese-containing acid phosphatase has been isolated and crystallized from sweet potato tubers. The pure enzyme contains one atom of manganese per Mr = 110,000 polypeptide and shows phosphatase activity toward various phosphate substrates. The pH optimum of the enzyme was 5.8 and the enzyme
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